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Q6NJJ2 (GSA_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate-1-semialdehyde 2,1-aminomutase

Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:hemL
Ordered Locus Names:DIP0409
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00375

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120404

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NJJ2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6B94BAA04DD5DE16

FASTA43045,362
        10         20         30         40         50         60 
MTSTQRSQEL FARAQQFTPG GVNSPVRAFG SVGGHARFIQ SAKGSKLYDV DGNEYVDLVC 

        70         80         90        100        110        120 
SWGPMLLGNA HPEIVEAVQK AATNGLSFGA PTEAEVKIAE MIVDRTSVEE VRMVNSGTEA 

       130        140        150        160        170        180 
TMSAVRLARG FTGRPKVIKF DGCYHGHVDA LLASAGSGVA TFALPDSPGV TGASAADTIV 

       190        200        210        220        230        240 
VPYNDSEAVR AAFEAHPDQI ACVIAEAAAG NMGTVAPQDN FNAKLKEVAH EHGALLILDE 

       250        260        270        280        290        300 
VMTGFRTSYN GWYGVDGVAG DLTTFGKVIS GGLPAAAFGG RADIMRYLAP EGPVYQAGTL 

       310        320        330        340        350        360 
SGNPVAMAAG MKSLELATPE VYDMVRANAD RLAGLLHEAL DREGVAHHIQ RAATMLSVRF 

       370        380        390        400        410        420 
AEGEGHNFDD MKAADTFRFP AFFHALLDNG IYASPSVFET WFVSAALTDD DFDKIEKALR 

       430 
PAAQAAGKAK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248355 Genomic DNA. Translation: CAE48913.1.
RefSeqNP_938790.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NJJ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP0409.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE48913; CAE48913; DIP0409.
GeneID2649362.
KEGGcdi:DIP0409.
PATRIC21481975. VBICorDip47633_0392.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARFMVSGN.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

UniPathwayUPA00251; UER00317.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00375. HemL_aminotrans_3.
InterProIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_CORDI
AccessionPrimary (citable) accession number: Q6NJJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways